4bt0: Difference between revisions

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<SX load='4bt0' size='340' side='right' viewer='molstar' caption='[[4bt0]], [[Resolution|resolution]] 17.00&Aring;' scene=''>
<SX load='4bt0' size='340' side='right' viewer='molstar' caption='[[4bt0]], [[Resolution|resolution]] 17.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4bt0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpmu Bpmu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BT0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=4BT0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4bt0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_Mu Escherichia virus Mu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BT0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BT0 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4bs1|4bs1]], [[4bt1|4bt1]]</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4bt0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bt0 OCA], [https://pdbe.org/4bt0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bt0 RCSB], [https://www.ebi.ac.uk/pdbsum/4bt0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bt0 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=4bt0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bt0 OCA], [http://pdbe.org/4bt0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4bt0 RCSB], [http://www.ebi.ac.uk/pdbsum/4bt0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4bt0 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[[https://www.uniprot.org/uniprot/O67198_AQUAE O67198_AQUAE]]
MuB is an ATP-dependent nonspecific DNA-binding protein that regulates the activity of the MuA transposase and captures target DNA for transposition. Mechanistic understanding of MuB function has previously been hindered by MuB's poor solubility. Here we combine bioinformatic, mutagenic, biochemical, and electron microscopic analyses to unmask the structure and function of MuB. We demonstrate that MuB is an ATPase associated with diverse cellular activities (AAA+ ATPase) and forms ATP-dependent filaments with or without DNA. We also identify critical residues for MuB's ATPase, DNA binding, protein polymerization, and MuA interaction activities. Using single-particle electron microscopy, we show that MuB assembles into a helical filament, which binds the DNA in the axial channel. The helical parameters of the MuB filament do not match those of the coated DNA. Despite this protein-DNA symmetry mismatch, MuB does not deform the DNA duplex. These findings, together with the influence of MuB filament size on strand-transfer efficiency, lead to a model in which MuB-imposed symmetry transiently deforms the DNA at the boundary of the MuB filament and results in a bent DNA favored by MuA for transposition.
 
MuB is an AAA+ ATPase that forms helical filaments to control target selection for DNA transposition.,Mizuno N, Dramicanin M, Mizuuchi M, Adam J, Wang Y, Han YW, Yang W, Steven AC, Mizuuchi K, Ramon-Maiques S Proc Natl Acad Sci U S A. 2013 Jun 17. PMID:23776210<ref>PMID:23776210</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4bt0" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</SX>
</SX>
[[Category: Bpmu]]
[[Category: Escherichia virus Mu]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Adam, J]]
[[Category: Adam J]]
[[Category: Dramicanin, M]]
[[Category: Dramicanin M]]
[[Category: Han, Y W]]
[[Category: Han YW]]
[[Category: Mizuno, N]]
[[Category: Mizuno N]]
[[Category: Mizuuchi, K]]
[[Category: Mizuuchi K]]
[[Category: Mizuuchi, M]]
[[Category: Mizuuchi M]]
[[Category: Ramon-Maiques, S]]
[[Category: Ramon-Maiques S]]
[[Category: Steven, A C]]
[[Category: Steven AC]]
[[Category: Wang, Y]]
[[Category: Wang Y]]
[[Category: Yang, W]]
[[Category: Yang W]]
[[Category: Aaa+ atpase]]
[[Category: Dna transposition]]
[[Category: Nucleoprotein filament]]
[[Category: Symmetry mismatch]]
[[Category: Transcription]]

Revision as of 17:06, 7 September 2022

MuB is an AAAplus ATPase that forms helical filaments to control target selection for DNA transposition

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